ID A0A151X1T0_9HYME Unreviewed; 3999 AA.
AC A0A151X1T0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Sortilin-related receptor {ECO:0000256|ARBA:ARBA00013467};
DE AltName: Full=Low-density lipoprotein receptor relative with 11 ligand-binding repeats {ECO:0000256|ARBA:ARBA00029896};
DE AltName: Full=Sorting protein-related receptor containing LDLR class A repeats {ECO:0000256|ARBA:ARBA00032450};
GN ORFNames=ALC60_06918 {ECO:0000313|EMBL:KYQ54371.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ54371.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ54371.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ54371.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ54371.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004212}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004212}. Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004158}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004158}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004115}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004530}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004530}. Endosome, multivesicular body membrane
CC {ECO:0000256|ARBA:ARBA00004545}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004545}. Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004614}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004614}. Golgi apparatus, trans-Golgi network
CC membrane {ECO:0000256|ARBA:ARBA00004393}; Single-pass type I membrane
CC protein {ECO:0000256|ARBA:ARBA00004393}. Recycling endosome membrane
CC {ECO:0000256|ARBA:ARBA00004480}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004480}.
CC -!- SIMILARITY: Belongs to the VPS10-related sortilin family. SORL1
CC subfamily. {ECO:0000256|ARBA:ARBA00007041}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR EMBL; KQ982585; KYQ54371.1; -; Genomic_DNA.
DR STRING; 64791.A0A151X1T0; -.
DR Proteomes; UP000075809; Unassembled WGS sequence.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030658; C:transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProt.
DR CDD; cd00063; FN3; 3.
DR CDD; cd00112; LDLa; 9.
DR Gene3D; 2.10.70.80; -; 1.
DR Gene3D; 3.30.60.270; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 9.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR000033; LDLR_classB_rpt.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR031777; Sortilin_C.
DR InterPro; IPR031778; Sortilin_N.
DR InterPro; IPR006581; VPS10.
DR PANTHER; PTHR12106; SORTILIN RELATED; 1.
DR PANTHER; PTHR12106:SF27; VPS10 HOMOLOG 1-RELATED; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00057; Ldl_recept_a; 9.
DR Pfam; PF00058; Ldl_recept_b; 2.
DR Pfam; PF15902; Sortilin-Vps10; 1.
DR Pfam; PF15901; Sortilin_C; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00192; LDLa; 9.
DR SMART; SM00135; LY; 5.
DR SMART; SM00602; VPS10; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 9.
DR SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 1.
DR SUPFAM; SSF63825; YWTD domain; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS01209; LDLRA_1; 4.
DR PROSITE; PS50068; LDLRA_2; 9.
DR PROSITE; PS51120; LDLRB; 3.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; EGF-like domain {ECO:0000256|ARBA:ARBA00022536};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Endosome {ECO:0000256|ARBA:ARBA00022753};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000313|EMBL:KYQ54371.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075809};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..3999
FT /note="Sortilin-related receptor"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007591616"
FT TRANSMEM 2103..2126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2197..2214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 3663..3685
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 823..866
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 916..961
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT REPEAT 962..1006
FT /note="LDL-receptor class B"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00461"
FT DOMAIN 1517..1611
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1615..1704
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1709..1798
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1799..1893
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 53..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2149..2190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2462..2516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2604..2640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2892..2911
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2956..2982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3288..3310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3334..3399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3557..3603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3920..3940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2482..2509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2606..2636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2956..2979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3334..3370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3560..3576
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3577..3593
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1110..1122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1117..1135
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1129..1144
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1149..1161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1156..1174
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1168..1183
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1188..1200
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1195..1213
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1207..1222
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1251..1266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1295..1310
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1329..1341
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1336..1354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1348..1363
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1385..1397
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1392..1410
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1404..1419
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1446..1461
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1472..1484
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1479..1497
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1491..1506
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 3999 AA; 448096 MW; 1F227D8891DCEDCA CRC64;
MAGRSSTALY YYFALILHLV LLTECDYNVR YGDKAKQLHV AEHNDQRYRK PLVIDRRSAD
LHERDDSDRK TSFGRTRRDV PLPQHPNNNP NITAKVNPLN DSHQQLMVHW VGDGSNVIIC
LARDSTPVVR FQGGKFSSPN QPSAVYISYD YGDSFENKTE HFRVSSEADA PYAVVDKFTN
HPKYYQHCVF MDSLNSLIFI TYNNGLTILR ISLSFHPSEV SYFELDPRIL VALDKTDLSR
KLWLTIDRGF TWMPIHQFVK AFFWSPYREL LVERMEPDGA NTVLKLDLRN ISSFIRGNNQ
LRARMSIRKE FIVVIENVED FQIRGDFMFA VKKRNGTEHL DLFVSYKNQT FVQAHFNTEL
DCKEYHIVDV SFNRVFIAVK HGDTMINLYV SEVIDHEKAI FTLSLESILT FFPNSTWKDS
WLNDVADETF TDLYKVEGLR GIYIASRVKG TPKSSSIGSE NLESLITFDH GATWNSIKAP
MANHEGFYIH CGKDCSLHLS QRFSQLYPVT RSVTIMSSKS APGMIMATGV IGSSLKGHPA
LYVSRDAGLT WKQVLKDYYF FNMGDHGGLL VAVKYFKSRG ETRDISYSTD EGETWQTYEF
NEKMLRVYGL MTEPGENTTV FTMFGSDSGQ HQWLIIKIDL RNVFERECTE DDYKFWSPTS
TDQPVMACVL GRKETYQRRA LRSNCYQGIN YFREIKLETC QCDANDYQCA YGFIPSGNPY
HCIHNKTMPD YDPYAVPTSC QPGMFYNRTK GYIKISDDDC TGGLAKNYEP DEIPCPMDES
PDFLLVAQRE HITRIDLVEN KLKKLPVHDL KNVIAIEFDM KNNCLYWADI VNDTIGRQCL
NGTSYPEILV ETDLSSIEGM AFDWVSKVLY FVDGVKMRIQ IIRTDVGPSI GRMRRTILGP
NNLQKPRGIA VHPMSGYMFW TDWAPGNASV SRANLDGTDV KRLFLKPTVE WPNGITIDHI
AERIYWVDAR LDYIASSDLE GKRFKNIIVK EARITHPFAV AVFKDNLYWD DWKQSMIFVA
DKDHGIGINT VLGFQIAGLM DLKIFAHSVQ VGTNDCAKNN TCSHICLGAP HSSHVCLCPD
GMVMTEGTCL CPGGIKPYSN STCPRVASTC SSNQFACNNN VCIPEFWKCD GDNDCGDNSD
EIQCNRATCS PNNFECDDNK CIPKYWVCDL DRDCKDGKDE MNCTYSNCTE TQFKCHNGRC
ISHRWRCDGE DDCRDGSDEL NCTKNIQPNT CRSDEIVCKT DHSCIPTSWK CDGEPDCEDS
ADEKDCNNMV CESWQFTCNN TKENGHRCIY KSWACDGDKD CIDGSDEVNC TTTTTLPTSI
IPILPTNSCN DWMFMCNNKK CVPYWWKCDS VDDCGDDSDE IGCGNTDGVL EPTSPVHTTQ
QSRICREHQF QCYNGECIEN AWVCDGLKDC PSGEDEQHCD HRHTCRENDQ FMCRQDGSCV
SLSSMCNGVE ECPDGSDELG CHAGELPATP SCYAGLFPCD ESRCFPLAAM CDGNRDCLDG
FDENHCEKNN SRVYQVLVMG VDERSINDTS LYLFWWMPIP SNVTFEFLPS IARVIPGAVW
TNATEWIEDT EYQFNNLEPF TKYNLTVYVR AKGQSDVSPP AKYHMVMTGE GVPSEPWNVK
VAQKNGTRVE VTWRPPLHPN GAISGYLGYV TPPIPPLEFI RSKTSATIDM AFEAGKNYSF
WIVAKNQHYN SVSSQVVTLT FDGTANIDDI ENLRVVTTTN HSVTLTWKKM QNVDGYHITP
RASPNYPNLQ TVTTLNSLME VDKLAPGTKY TFEVGAMKKN YVGKVTSVTA TTNGTALPTI
NNFDAQLVKS QRTTVKLTWD PPKSTRKIKW KYAIHYAVNM EDFFKSAKHI TTNLTATIKD
LEACEAYFFA VGVIGDYGAG PLNQPHTVTT HFNKRAPPKK LRVAPSPNEN DSMIVSWMSS
CPAVDEIISY TISVTEMIMN KHIVVTLPPT NETVMKHIFY SIKYGGTYNI TIATDVENAI
STQPFIYIAP PIKPPHQLTV LHDNMEYLIY WKEPDLPENI KKDTDRYFEI LVAEGSRTIN
ESTAKVLVVK DPPYRYKDAK TDTIYTFAAR LVTNEGYQSP LSETWSTQIS GSQLPVIMNT
SGILSLAIPI CLVVIALGAA LAYFIVRHRR LSHSFTQFAN SHYDTRRGQA TFPGATDGLE
EEDSPVIRGF SDDEPLPPYP SPDTGPLSNN DGRSAKMRMQ LLKIVVVLLV AGSGDTRPQN
GADSQAKTIE RNDAGWRGIQ VSSKSHDIVR DDSRYTGTSG SNRKYITHFR DSADSSREHN
TVANARSLSV RRSKIDDIWT MPKFRAINAP PYFSRTDVLG GIAKFATVVQ NSNEVNKPSF
HASSGDSKII QNERINWTRF SSDSKNAGNL ERSKSGVISN ENLDPITQTK YSYGAGNDFL
ATHASGFERT NDDISVAVEN RRKSSSVRFD SFVNKDVEGE MSRWKQGVNR FSLQIARTNV
PRDSQANAST HSIHKDRNSI RKTTNSSVIS HGNSKPSVVI NSSRSIGDHG DLNNSERSAH
DAKTVLIPNS KFEIVGQSPA FRRRNATTSH RNFVKLRYPY STLNWRNVSN VALNMKMKNG
NNIFTDIQLR KPVKHFTRIG AKKPVSLNNH VTSKPMKSNH SSSVQESPSQ KVGSENRTVD
KYNDTTLHDA YLKNWPNDAI QDFEDLYNYE KYTSSLEEES SHESSLSSAE EIPILSSNNY
FDHSDPILDS SVKKIIHWLK VPEIVPNNTQ YFDHDDDKPI ESNYESIYEN LEPNSPLNTN
THDDNYDTVV LQDVPLSQNL DTIDSNYPIR WSNPSSITSL QYETDSSNPS APLIPSFWPG
GALLQNKTVY NPTTHVTQNT VVHILNDGLK KPNVTRLKAS EANAAAANQA TSSGSSSESL
VQIPNVMFTS QKDENKNISK QETDTFPSST YNTNCPTIMI NTYTRVNNTL QSKEGCTDLN
IIVNSHVLNT NVFKPSSAPA TAEDHQTSLT TQNYGSADES EEYSDVLTDL SHVDSLAASA
SASGPPVAGT PVSENPSVPV AQELPVYLIK PGPVTGQSSA GLGSLQLSAL PNLPSLNIAT
KPDLSSSAGS SFGQVNDTHR DLKDLQYMDQ SLRTVATQLL NVTNPQDMVN VNNKELIKAE
HNVATTPKSS ENSVPLLMRD VSSEINLEPV HFGRPINSKF SYFESSHPGQ AMAMTEEELE
REISTTRLIT AYKNHPTTTG GISTWILLNP PSTTVKSVEI EKSKTQQPFQ TEVRLTVRPS
SSIEKETIPQ PEKITEKTTP QLTPVITTEK VTVITKKPSM TTTKKIVTTS KPEKVTQNSE
KTESSSSTTL KVIRTTTTST STTSDGTATL TAVLTTKKSQ SPRTTSKPKV TTSRTTLHSK
PATTKPASIK PTTMKPVRPK PTRKSTVKPE TIKNDTSTST GKIEKVTFKP VSVITTPQDK
LENTEKPMFV TKIKASVLMD TQKTPTTLLP ATTATTLSAS TTFKSNFSTV DLVEVPVKSK
PVNTKGNNVL KVQLKKPIDE TTQIEIQPIK VNAPILTIEK IDKMDEIMMK DMDDLNDSRI
DLKFDFNPEL TKINVETKAE ADAMTSTSAT ASTTTKRPRH NSKRKKNKTR RRKPTTTSPS
STMVPVLMET NESVTDSTIT DNAVQESKIA PETKVGANTT KTKKKQPQKA ISTQIYNFLS
REVMPSFGVM SLVGLGLGLA SYFLYPFGGT ITRRNYDVEP NYKYNMDEYG GNYGQSEEEM
LSKVYQGMTN YENKYPGTKD NYNSNYYQYQ HYDGAYDTQT KKIETRYPSV TTSPVYKAVE
NTQPAVKYRN TDFQYPEAQT TPVYYDRKRL DFATEVGTSS AANRQFVVGN VPKEYPFDVK
AANLPVDNKK GYMSTEVGQT QFEREVTQDF DFPNAAGLNS YGHLGASTIR ADDGYEEIEI
TPTAVAVEHG PRSLKVKRAA LNEEKSSDTT HPADSKDPET IEWFDSSTTK KPSEGFSLIN
FVKKVAEIKF RLGLTILKHA SEGFARYLGH VQKRINGEE
//
